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Direct observation of peptide hydrogel self-assembly.

Zoë C Adams1, Erika J Olson1, Tania L Lopez-Silva2

  • 1Department of Chemistry, The Scripps Research Institute 10550 North Torrey Pines Road La Jolla California 92037 USA dawson@scripps.edu.

Chemical Science
|September 21, 2022
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Summary

Transparent window infrared (IR) spectroscopy with carbon-deuterium (C-D) probes tracks the rapid self-assembly of MAX1 peptide hydrogels. This method reveals MAX1 peptide self-assembly as a cooperative process, offering insights into drug delivery materials.

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Area of Science:

  • Biophysical Chemistry
  • Spectroscopy
  • Materials Science

Background:

  • Characterizing self-assembling molecules, particularly those prone to phase separation or precipitation, poses experimental difficulties.
  • Transparent window infrared (IR) spectroscopy utilizes site-specific probes, such as carbon-deuterium (C-D) bonds, which are non-perturbative and sensitive to the local molecular environment.
  • IR spectroscopy's applicability to diverse sample states makes it suitable for studying challenging self-assembling systems.

Purpose of the Study:

  • To demonstrate the application of time-resolved transparent window IR spectroscopy for observing the continuous dynamics of self-assembling molecules.
  • To investigate the self-assembly process of the MAX1 peptide hydrogel, a promising biocompatible material for drug delivery.
  • To determine site-specific kinetic information during the self-assembly of the MAX1 peptide.

Main Methods:

  • Synthetically incorporated C-D labeled valine into five specific positions of the MAX1 β-hairpin peptide.
  • Utilized stopped-flow initiation coupled with transparent window Fourier Transform Infrared (FTIR) spectroscopy to monitor C-D bond absorption frequencies and linewidths over time.
  • Analyzed spectral changes following a rapid ionic strength jump to initiate peptide self-assembly.

Main Results:

  • Steady-state IR spectra confirmed that C-D labeled side chains reside in a hydrophobic environment within the MAX1 hydrogel.
  • Analysis indicated restricted motion for side chains in the peptide's middle compared to its ends.
  • Time-resolved measurements revealed that MAX1 peptide self-assembly occurs as a cooperative process within experimental resolution.

Conclusions:

  • Stopped-flow transparent window FTIR spectroscopy is a viable technique for real-time observation of molecular self-assembly dynamics.
  • The study provides kinetic insights into the cooperative self-assembly of the MAX1 peptide hydrogel.
  • This methodology holds potential for broader applications in studying dynamic biological processes like protein folding and enzyme kinetics.